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Database: UniProt
Entry: L5_FOWPN
LinkDB: L5_FOWPN
Original site: L5_FOWPN 
ID   L5_FOWPN                Reviewed;         129 AA.
AC   P15914;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   02-JUN-2021, entry version 73.
DE   RecName: Full=L5 homolog;
DE   AltName: Full=Protein FPV132;
GN   OrderedLocusNames=FPV132; ORFNames=FP6;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-444;
RX   PubMed=2838574; DOI=10.1099/0022-1317-69-6-1275;
RA   Binns M.M., Tomley F.M., Campbell J., Boursnell M.E.G.;
RT   "Comparison of a conserved region in fowlpox virus and vaccinia virus
RT   genomes and the translocation of the fowlpox virus thymidine kinase gene.";
RL   J. Gen. Virol. 69:1275-1283(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Salisbury;
RX   PubMed=2820129; DOI=10.1016/0042-6822(87)90061-4;
RA   Drillien R., Spehner D., Villeval D., Lecocq J.-P.;
RT   "Similar genetic organization between a region of fowlpox virus DNA and the
RT   vaccinia virus HindIII J fragment despite divergent location of the
RT   thymidine kinase gene.";
RL   Virology 160:203-209(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
CC   -!- FUNCTION: Envelope protein part of the entry-fusion complex responsible
CC       for the virus membrane fusion with host cell membrane during virus
CC       entry. Also plays a role in cell-cell fusion (syncytium formation) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at least
CC       composed of proteins A16, A21, A28, G3, G9, H2, J5, and L5. Formation
CC       of the viral membrane is necessary for the assembly of the complex.
CC       Interacts with G3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type
CC       III membrane protein {ECO:0000305}. Note=Component of the mature virion
CC       (MV) membrane (By similarity). The mature virion is located in the
CC       cytoplasm of infected cells and is probably released by cell lysis.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Most cysteines are linked by disulfide bonds. They are created by
CC       the viral disulfide bond formation pathway, a poxvirus-specific redox
CC       pathway that operates on the cytoplasmic side of the MV membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae L5 family. {ECO:0000305}.
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DR   EMBL; D00320; BAA00229.1; -; Genomic_DNA.
DR   EMBL; M17418; AAA66420.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44476.1; -; Genomic_DNA.
DR   PIR; JS0226; WMVZP6.
DR   RefSeq; NP_039095.1; NC_002188.1.
DR   GeneID; 1486680; -.
DR   KEGG; vg:1486680; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR006956; Poxvirus_L5.
DR   Pfam; PF04872; Pox_L5; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Fusion of virus membrane with host cell membrane;
KW   Fusion of virus membrane with host membrane; Late protein; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..129
FT                   /note="L5 homolog"
FT                   /id="PRO_0000099629"
FT   TRANSMEM        27..47
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  14745 MW;  DB98CCC282E48A6B CRC64;
     MDRNINFSPV FIEPRFKHEF LLSPQRYFYI LVFEVIVALI ILNFFFKEEI LYTFFPLAKP
     SKNSINSLLD RTMLKCEEDG SLMISRPSGI YSALSLDGSP VRISDCSLLL SSINGASSST
     SPYSIFNRR
//
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